INVESTIGADORES
FERNANDEZ Claudio Oscar
artículos
Título:
Exploring the Structural Details of Cu(I) Binding to á-Synuclein by NMR Spectroscopy
Autor/es:
ANDRES BINOLFI; ARIEL A. VALIENTE-GABIOUD; ROSARIO DURAN; MARKUS ZWECKSTETTER; CHRISTIAN GRIESINGER; CLAUDIO O. FERNANDEZ
Revista:
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Editorial:
AMER CHEMICAL SOC
Referencias:
Lugar: Washington; Año: 2010 vol. 133 p. 194 - 196
ISSN:
0002-7863
Resumen:
The aggregation of alpha-synuclein (AS) is selectively
enhanced by copper in vitro, and the interaction is proposed to
play a potential role in vivo. In this work, we report the structural,
residue-specific characterization of Cu(I) binding to AS and
demonstrate that the protein is able to bind Cu(I) with relatively
high affinity in a coordination environment that involves the
participation of Met1 and Met5 residues. This knowledge is a key
to understanding the structural-aggregation basis of the copper catalyzed
oxidation of AS.
enhanced by copper in vitro, and the interaction is proposed to
play a potential role in vivo. In this work, we report the structural,
residue-specific characterization of Cu(I) binding to AS and
demonstrate that the protein is able to bind Cu(I) with relatively
high affinity in a coordination environment that involves the
participation of Met1 and Met5 residues. This knowledge is a key
to understanding the structural-aggregation basis of the copper catalyzed
oxidation of AS.
The aggregation of alpha-synuclein (AS) is selectively
enhanced by copper in vitro, and the interaction is proposed to
play a potential role in vivo. In this work, we report the structural,
residue-specific characterization of Cu(I) binding to AS and
demonstrate that the protein is able to bind Cu(I) with relatively
high affinity in a coordination environment that involves the
participation of Met1 and Met5 residues. This knowledge is a key
to understanding the structural-aggregation basis of the copper catalyzed
oxidation of AS.